{"doi":"10.1128/ec.05253-11","title":"The Ubiquitin Ligase Ubr11 Is Essential for Oligopeptide Utilization in the Fission Yeast Schizosaccharomyces pombe","abstract":"<jats:title>ABSTRACT</jats:title>\n          <jats:p>\n            Uptake of extracellular oligopeptides in yeast is mediated mainly by specific transporters of the peptide transporter (PTR) and oligopeptide transporter (OPT) families. Here, we investigated the role of potential peptide transporters in the yeast\n            <jats:named-content content-type=\"genus-species\">Schizosaccharomyces pombe</jats:named-content>\n            . Utilization of naturally occurring dipeptides required only Ptr2/SPBC13A2.04c and none of the other 3 OPT proteins (Isp4, Pgt1, and Opt3), whereas only Isp4 was indispensable for tetrapeptide utilization. Both Ptr2 and Isp4 localized to the cell surface, but under rich nutrient conditions Isp4 localized in the Golgi apparatus through the function of the ubiquitin ligase Pub1. Furthermore, the ubiquitin ligase Ubr11 played a significant role in oligopeptide utilization. The mRNA levels of both the\n            <jats:italic>ptr2</jats:italic>\n            and\n            <jats:italic>isp4</jats:italic>\n            genes were significantly reduced in\n            <jats:italic>ubr11</jats:italic>\n            Δ cells, and the dipeptide utilization defect in the\n            <jats:italic>ubr11</jats:italic>\n            Δ mutant was rescued by the forced expression of Ptr2. Consistent with its role in transcriptional regulation of peptide transporter genes, the Ubr11 protein was accumulated in the nucleus. Unlike the situation in\n            <jats:named-content content-type=\"genus-species\">Saccharomyces cerevisiae</jats:named-content>\n            , the oligopeptide utilization defect in the\n            <jats:named-content content-type=\"genus-species\">S. pombe</jats:named-content>\n            <jats:italic>ubr11</jats:italic>\n            Δ mutant was not rescued by inactivation of the Tup11/12 transcriptional corepressors, suggesting that the requirement for the Ubr ubiquitin ligase in the upregulation of peptide transporter mRNA levels is conserved in both yeasts; however, the actual mechanism underlying the control appears to be different. We also found that the peptidomimetic proteasome inhibitor MG132 was still operative in a strain lacking all known PTR and OPT peptide transporters. Therefore, irrespective of its peptide-like structure, MG132 is carried into cells independently of the representative peptide transporters.\n          </jats:p>","journal":"Eukaryotic Cell","year":2012,"id":36783,"datarank":0.6904928808378928,"base_score":2.70805020110221,"endowment":2.70805020110221,"self_citation_contribution":0.40620753016533157,"citation_network_contribution":0.2842853506725613,"self_endowment_contribution":0.40620753016533157,"citer_contribution":0.2842853506725613,"corpus_percentile":null,"corpus_rank":null,"citation_count":14,"citer_count":8,"citers_with_citation_signal":8,"citers_with_endowment":8,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":185650,"name":"Mai Nakase","orcid":null,"position":1,"is_corresponding":false},{"id":185651,"name":"Hideki Tohda","orcid":null,"position":2,"is_corresponding":false},{"id":185652,"name":"Kaoru Takegawa","orcid":null,"position":3,"is_corresponding":false},{"id":185649,"name":"Kenji Kitamura","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"base_score":2.639057329615259,"endowment":2.639057329615259,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"22226946","pmcid":"PMC3294451","openalex_id":"https://openalex.org/W2032125488","authors":[],"funders":[],"total_grants":0,"fwci":1.2091,"citation_percentile":0.77659069,"influential_citations":0,"citation_trend":[{"year":2012,"count":2},{"year":2014,"count":5},{"year":2015,"count":2},{"year":2016,"count":1},{"year":2020,"count":2},{"year":2024,"count":1}],"oa_status":"gold","license":"https://journals.asm.org/non-commercial-tdm-license","oa_locations":[{"url":"https://ec.asm.org/content/eukcell/11/3/302.full.pdf","host_type":"journal"},{"url":"https://ec.asm.org/content/eukcell/11/3/302.full.pdf","host_type":"GOLD"},{"url":"https://ec.asm.org/content/eukcell/11/3/302.full.pdf","host_type":"publisher"},{"url":"https://journals.asm.org/doi/pdf/10.1128/EC.05253-11","host_type":"publisher"},{"url":"https://doi.org/10.1128/ec.05253-11","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/22226946","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/3294451","host_type":"repository"}],"fields_of_study":["Fungal and yeast genetics research","Ubiquitin and proteasome pathways","14-3-3 protein interactions","Biology","Medicine","Cysteine Proteinase Inhibitors","Gene Deletion","Gene Expression Regulation, Fungal","Genetic Complementation Test","Leupeptins","Membrane Transport Proteins","Oligopeptides","Proteasome Endopeptidase Complex","Proteasome Inhibitors","Protein Transport","Saccharomyces cerevisiae","Saccharomyces cerevisiae Proteins","Schizosaccharomyces","Schizosaccharomyces pombe Proteins","Ubiquitin-Protein Ligases"],"mesh_terms":["Genetic Complementation Test","Leupeptins","Oligopeptides","Saccharomyces cerevisiae","Schizosaccharomyces","Cysteine Proteinase Inhibitors","Gene Expression Regulation, Fungal","Gene Deletion","Protein Transport","Membrane Transport Proteins","Saccharomyces cerevisiae Proteins","Schizosaccharomyces pombe Proteins","Ubiquitin-Protein Ligases","Proteasome Endopeptidase Complex","Proteasome Inhibitors"],"keywords":["Schizosaccharomyces pombe","Schizosaccharomyces","Yeast","Ubiquitin ligase","Biology","Oligopeptide","Fission","DNA ligase","Ubiquitin","Cell biology","Genetics","Biochemistry","Saccharomyces cerevisiae","Gene","Physics","Peptide"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-06-10T17:24:24.091522Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}